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C1DMY5 (GSA_AZOVD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate-1-semialdehyde 2,1-aminomutase

Short name=GSA
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name=GSA-AT
Gene names
Name:hemL
Ordered Locus Names:Avin_09260
OrganismAzotobacter vinelandii (strain DJ / ATCC BAA-1303) [Complete proteome] [HAMAP]
Taxonomic identifier322710 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Protein attributes

Sequence length429 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate. HAMAP-Rule MF_00375

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00375

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2. HAMAP-Rule MF_00375

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00375

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00375.

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutamate-1-semialdehyde 2,1-aminomutase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

transaminase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 429429Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382256

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C1DMY5 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 58602B750BEA4873

FASTA42945,276
        10         20         30         40         50         60 
MSRSETLFAN AQKHIPGGVN SPVRAFRGVG GTPLFFKHAE GAYVIDEDDK RYVDYVGSWG 

        70         80         90        100        110        120 
PMILGHAHPD VLEAVRRQLE HGLSYGAPTA LETEMAELVC SLVPSMDMVR MVSSGTEATM 

       130        140        150        160        170        180 
SAIRLARGYT GRDSIIKFEG CYHGHSDSLL VKAGSGALTL GVPSSPGVPA AFAKHTLTLP 

       190        200        210        220        230        240 
YNDLGAVEKT LAEVGREIAC IIVEPVAGNM NCVPPAPGFL EGLRAQCDQH GVVLIFDEVM 

       250        260        270        280        290        300 
TGFRVALGGA QAHYGVTPDL STFGKIVGGG MPVGCFGGKR AIMECIAPLG PVYQAGTLSG 

       310        320        330        340        350        360 
NPLAMAAGLT TLKLIGRPGF HRELAEYTGR LLQGLQERAD AAGIPFVTTQ AGGMFGLYFS 

       370        380        390        400        410        420 
GADEIVTFAD VMASDAERFK RFFHLMLDGG VYLAPSAFEA GFTSIVHGET ELSITLEAAE 


RAFATLAKA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001157 Genomic DNA. Translation: ACO77165.1.
RefSeqYP_002798140.1. NC_012560.1.

3D structure databases

ProteinModelPortalC1DMY5.
SMRC1DMY5. Positions 2-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING322710.Avin_09260.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO77165; ACO77165; Avin_09260.
GeneID7759874.
KEGGavn:Avin_09260.
PATRIC21028145. VBIAzoVin72790_0865.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycAVIN322710:GJ0M-927-MONOMER.
UniPathwayUPA00251; UER00317.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPMF_00375. HemL_aminotrans_3.
InterProIPR004639. 4pyrrol_synth_GluAld_NH2Trfase.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR00713. hemL. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSA_AZOVD
AccessionPrimary (citable) accession number: C1DMY5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: May 26, 2009
Last modified: May 14, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways